ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Porcine trypsin (EC 3.4.4.4) converted, within approximately 2 hr at 50°C, its 1000-fold weight of water-insoluble, heat-denaturated cheese whey protein into a water-soluble product. In the course of this digestion, the enzyme increased the α-amino nitrogen of the protein by a factor of 〉20, from 0.40 to 9.40%. After digesting the water-insoluble whey protein, fully active trypsin could be recovered from the soluble digest with the aid of a cellulose-based affinity adsorbent. The enzyme which was eluted from a column of p-aminobenzamidine, bound to succinylated aminododecylcellulose, was fully active and showed essentially unchanged kinetic properties with a synthetic substrate, L-benzoyl-arginine p-nitroanilide. It was possible to perform, with the same amount of trypsin, three subsequent and equally effective solubilizations of whey protein, followed by a fourth digestion which still yielded a soluble product, but was considerably slower and incomplete. During each digestion, an estimated 30% of the trypsin was lost. The was not due to a decreased efficiency of the affinity adsorbent, as its trypsin-binding capacity was essentially unaffected after over 10 cycles of use.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260200805
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